ID Q1IRH4_KORVE Unreviewed; 766 AA.
AC Q1IRH4;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Acid345_1524 {ECO:0000313|EMBL:ABF40526.1};
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Koribacter.
OX NCBI_TaxID=204669 {ECO:0000313|EMBL:ABF40526.1, ECO:0000313|Proteomes:UP000002432};
RN [1] {ECO:0000313|EMBL:ABF40526.1, ECO:0000313|Proteomes:UP000002432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345 {ECO:0000313|EMBL:ABF40526.1,
RC ECO:0000313|Proteomes:UP000002432};
RX PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000360; ABF40526.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1IRH4; -.
DR STRING; 204669.Acid345_1524; -.
DR EnsemblBacteria; ABF40526; ABF40526; Acid345_1524.
DR KEGG; aba:Acid345_1524; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_5_2_0; -.
DR Proteomes; UP000002432; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00731; CheA_reg; 1.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 2.40.50.180; CheA-289, Domain 4; 1.
DR Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR037006; CheA-like_homodim_sf.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 2.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 2.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ABF40526.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000002432};
KW Transferase {ECO:0000313|EMBL:ABF40526.1}.
FT DOMAIN 14..118
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 215..465
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 467..604
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 627..758
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 147..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 766 AA; 82744 MW; B79F451406626667 CRC64;
MVQVARSGTD GHDGMSEMDE IVKEFLVESN EGLDQLDRDL VALEKDPEEK DLLASIFRAI
HTVKGTSGVL GFPKIESVAH VGESLLSRLR DGKMRLDPQI TSGLLAMGDV LRELLGNIDA
LGVEGDRNVE PVVTRLSALL ERTDSSKAAD AATADTAPEA RKKTTKRVAK KRSKAAVEPL
SVAEASPAPA STLAADEAAQ SGANLETSEA RGPAVSANNI RVDVGLLDKM MNLVGELVLA
RNQILQYTGS QQDSGFVSAA QRLNLITTEL QESVMKTRMQ PIGNIWNKLP RLVRDLALSC
GKQVRVEMDG AETELDKTII EAIKDPLTHI VRNAVDHGLE MPEERRSTGK EAEGRLLLRA
YHEGGQVNIE ISDDGKGVDL EAVREKARQR GLVSAEQAAR MSERELLNVL FLPGFSTAKQ
VTNISGRGVG MDVVKTNIEK IGGTVDLQSV EGKGTALKIK IPLTLAIIPA LIATSGGERF
AIPQVSLLEL VRLEGDGVGK GIEYIHGAPV YRLRGSLLPL VSLNGVLGLD RKKQQEIANI
VVLQADDRTF GLIVDEINDT EEIVVKPLSN LLKGLLCFAG ATIMGDGTVA LILDVMGLAQ
QASVVTELRD RAVKQMHARN EDGRMESEAW LLTRVGEEGR IAVPLSNVNR LEEFKLSSVE
HSGGLEVVQY RGQIMPLVRL SQLLNLPGTD AGEVLPVIVT SQQGRSLGLV VDKIEDVTEQ
QIAVNRSNDR MYLQGSAVLQ QRVTDLLDVH AVMASVCTEF KEVVNA
//
